TRMD_AQUAE
ID TRMD_AQUAE Reviewed; 257 AA.
AC O67463;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase;
DE EC=2.1.1.228;
DE AltName: Full=M1G-methyltransferase;
DE AltName: Full=tRNA [GM37] methyltransferase;
GN Name=trmD; OrderedLocusNames=aq_1489;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=14517984; DOI=10.1002/prot.10479;
RA Liu J., Wang W., Shin D.H., Yokota H., Kim R., Kim S.-H.;
RT "Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus
RT at 2.6 A resolution: a novel methyltransferase fold.";
RL Proteins 53:326-328(2003).
CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14517984}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07418.1; -; Genomic_DNA.
DR PIR; E70429; E70429.
DR RefSeq; NP_214028.1; NC_000918.1.
DR RefSeq; WP_010880966.1; NC_000918.1.
DR PDB; 1OY5; X-ray; 2.60 A; A/B/C=1-257.
DR PDBsum; 1OY5; -.
DR AlphaFoldDB; O67463; -.
DR SMR; O67463; -.
DR STRING; 224324.aq_1489; -.
DR EnsemblBacteria; AAC07418; AAC07418; aq_1489.
DR KEGG; aae:aq_1489; -.
DR PATRIC; fig|224324.8.peg.1161; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_0; -.
DR InParanoid; O67463; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR BRENDA; 2.1.1.228; 396.
DR EvolutionaryTrace; O67463; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR CDD; cd18080; TrmD-like; 1.
DR Gene3D; 1.10.1270.20; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00605; TrmD; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR46417; PTHR46417; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF000386; tRNA_mtase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00088; trmD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..257
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060317"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 134..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1OY5"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1OY5"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1OY5"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:1OY5"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1OY5"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1OY5"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1OY5"
SQ SEQUENCE 257 AA; 29652 MW; F03ACF8EE2D7EBD5 CRC64;
MSSNPLRFFV LTIFPHIISC YSEYGIVKQA IKKGKVEVYP IDLREFAPKG QVDDVPYGGL
PGMVLKPEPI YEAYDYVVEN YGKPFVLITE PWGEKLNQKL VNELSKKERI MIICGRYEGV
DERVKKIVDM EISLGDFILS GGEIVALAVI DAVSRVLPGV LSEPQSIQED SFQNRWLGYP
VYTRPREYRG MKVPEELLSG HHKLIELWKL WHRIENTVKK RPDLIPKDLT ELEKDILNSI
LSGKSFKEWL KEHKHLL
